Agency
National Institute of Health (NIH)
Institute
National Eye Institute (NEI)
Type
Research Project (R01)
Project #
5R01EY010011-03
Application #
2163711
Study Section
Visual Sciences C Study Section (VISC)
Project Start
1994-06-01
Project End
1998-02-28
Budget Start
1996-06-01
Budget End
1998-02-28
Support Year
3
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Rensselaer Polytechnic Institute
Department
Biology
Type
Schools of Arts and Sciences
DUNS #
002430742
City
Troy
State
NY
Country
United States
Zip Code
12180
Li, Ying; Schmitz, Karl R; Salerno, John C et al. (2007) The role of the conserved COOH-terminal triad in alphaA-crystallin aggregation and functionality. Mol Vis 13:1758-68
Yang, Chaoxing; Salerno, John C; Koretz, Jane F (2005) NH2-terminal stabilization of small heat shock protein structure: a comparison of two NH2-terminal deletion mutants of alphaA-crystallin. Mol Vis 11:641-7
Eifert, Cheryl; Burgio, Michael R; Bennett, Pauline M et al. (2005) N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function. Biochim Biophys Acta 1748:146-56
Regini, J W; Grossmann, J G; Burgio, M R et al. (2004) Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction. J Mol Biol 336:1185-94
Salerno, John C; Eifert, Cheryl L; Salerno, Kathleen M et al. (2003) Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region. Protein Eng 16:847-51
Desai, Prashant; Prachand, Mamta; Coutinho, Evans et al. (2002) Activity and conformation of a cyclic heptapeptide possessing the message sequence His-Phe-Arg-Trp of alpha-melanotropin. Int J Biol Macromol 30:187-95
Burgio, M R; Bennett, P M; Koretz, J F (2001) Heat-induced quaternary transitions in hetero- and homo-polymers of alpha-crystallin. Mol Vis 7:228-33
Burgio, M R; Kim, C J; Dow, C C et al. (2000) Correlation between the chaperone-like activity and aggregate size of alpha-crystallin with increasing temperature. Biochem Biophys Res Commun 268:426-32
Koretz, J F; Doss, E W; LaButti, J N (1998) Environmental factors influencing the chaperone-like activity of alpha-crystallin. Int J Biol Macromol 22:283-94
Doss-Pepe, E W; Carew, E L; Koretz, J F (1998) Studies of the denaturation patterns of bovine alpha-crystallin using an ionic denaturant, guanidine hydrochloride and a non-ionic denaturant, urea. Exp Eye Res 67:657-79

Showing the most recent 10 out of 13 publications